ReviewFEBS letters2009
Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification.
Review in FEBS letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates.International journal of molecular sciences · 2020Article
- Experimentally-driven protein structure modeling.Journal of proteomics · 2020Review
- Prion replication environment defines the fate of prion strain adaptation.PLoS pathogens · 2018Article
- Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Molecular psychiatry · 2018Article
- Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils.PloS one · 2018Article
- Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017Review
- Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.PLoS pathogens · 2017Article
- Perivascular Accumulation of β-Sheet-Rich Proteins in Offspring Brain following Maternal Exposure to Carbon Black Nanoparticles.Frontiers in cellular neuroscience · 2017Article
- Mammalian prion amyloid formation in bacteria.Prion · 2016Article
- Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.Microbial cell factories · 2015Article
- Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seeds.The Journal of biological chemistry · 2013Article
- Article
- Atomic force fluorescence microscopy in the characterization of amyloid fibril assembly and oligomeric intermediates.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease.PLoS pathogens · 2011Article
- Two amyloid States of the prion protein display significantly different folding patterns.Journal of molecular biology · 2010Article
- Emergence and natural selection of drug-resistant prions.Molecular bioSystems · 2010Review
- Complement protein C1q forms a complex with cytotoxic prion protein oligomers.The Journal of biological chemistry · 2010Article
- Coinfecting prion strains compete for a limiting cellular resource.Journal of virology · 2010Article
- Strain phenomenon in protein aggregation: Interplay between sequence and conformation.Intrinsically disordered proteinsArticle
- Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Amyloid fibrils are highly ordered crystal-like structures. It is generally assumed that individual amyloid fibrils consist of conformationally uniform cross-beta-sheet structures that enable the amyloids to replicate their individual conformations via a template-dependent mechanism. Recent studies revealed that amyloids are capable of accommodating a global conformational switch from one amyloid strain to another within individual fibrils. The current review highlights the high adaptation potential of amyloid structures and discusses the implication of these findings for several emerging issues including prion strain adaptation (i.e. gradual change in strain structure). It also proposes that the catalytic activity of an amyloid structure should be separated from its templating effect, and raises the question of strain classification according to their promiscuous or species-specific nature.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.